ArticleApplied and environmental microbiology2008
The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 49 citations in OpenAlex.
- Secretory Production of Mature Protein-Glutaminase from Bacteroides helcogenes in Bacillus subtilis.Applied biochemistry and biotechnology · 2026Article
- Toward food-grade production of the Bacteroides helcogenes protein-glutamine glutaminase with an optimized Bacillus subtilis strain.Applied microbiology and biotechnology · 2026Article
- Engineered Endosymbionts that Modulate Primary Macrophage Function and Attenuate Tumor Growth by Shifting the Tumor Microenvironment.ACS applied bio materials · 2025Article
- The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024Article
- Secretion of the cytoplasmic and high molecular weight β-galactosidase of Paenibacillus wynnii with Bacillus subtilis.Microbial cell factories · 2024Article
- Localization of Pyranose 2-Oxidase fromInternational journal of molecular sciences · 2023Article
- Engineered endosymbionts that alter mammalian cell surface marker, cytokine and chemokine expression.Communications biology · 2022Article
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Exploitation of Bacillus subtilis as a robust workhorse for production of heterologous proteins and beyond.World journal of microbiology & biotechnology · 2018Review
- Discovery of new cellulases from the metagenome by a metagenomics-guided strategy.Biotechnology for biofuels · 2016Article
- Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.The Journal of biological chemistry · 2014Article
- Article
- Fermentation stage-dependent adaptations of Bacillus licheniformis during enzyme production.Microbial cell factories · 2013Article
- The secretion of an intrinsically disordered protein with different secretion signals in Bacillus subtilis.Current microbiology · 2013Article
- High-salinity growth conditions promote Tat-independent secretion of Tat substrates in Bacillus subtilis.Applied and environmental microbiology · 2012Article
- Specific targeting of the metallophosphoesterase YkuE to the bacillus cell wall requires the twin-arginine translocation system.The Journal of biological chemistry · 2012Article
- Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.PloS one · 2011Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Proteins that are produced for commercial purposes in Bacillus subtilis are commonly secreted via the Sec pathway. Despite its high secretion capacity, the secretion of heterologous proteins via the Sec pathway is often unsuccessful. Alternative secretion routes, like the Tat pathway, are therefore of interest. Two parallel Tat pathways with distinct specificities have previously been discovered in B. subtilis. To explore the application potential of these Tat pathways, several commercially relevant or heterologous model proteins were fused to the signal peptides of the known B. subtilis Tat substrates YwbN and PhoD. Remarkably, the YwbN signal peptide directed secretion of active subtilisin, a typical Sec substrate, via the B. subtilis TatAyCy route. In contrast, the same signal peptide directed Tat-independent secretion of the Bacillus licheniformis alpha-amylase (AmyL). Moreover, the YwbN signal peptide directed secretion of SufI, an Escherichia coli Tat substrate, in a Tat-independent manner, most likely via Sec. Our results suggest that cytoplasmic protein folding prior to translocation is probably a major determinant of Tat-dependent protein secretion in B. subtilis, as is the case with E. coli. We conclude that future applications for the Tat system of B. subtilis will most likely involve commercially interesting proteins that are Sec incompatible.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.